PME30_ARATH
ID PME30_ARATH Reviewed; 497 AA.
AC Q3EAY9; A0MFT0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable pectinesterase 30;
DE Short=PE 30;
DE EC=3.1.1.11;
DE AltName: Full=Pectin methylesterase 30;
DE Short=AtPME30;
DE Flags: Precursor;
GN Name=PME30; Synonyms=ARATH30; OrderedLocusNames=At3g27980;
GN ORFNames=K24A2.9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15337457; DOI=10.1016/j.carres.2004.06.023;
RA Markovic O., Janecek S.;
RT "Pectin methylesterases: sequence-structural features and phylogenetic
RT relationships.";
RL Carbohydr. Res. 339:2281-2295(2004).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16622707; DOI=10.1007/s00425-006-0261-9;
RA Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F.,
RA Guerineau F., Pelloux J.;
RT "Comprehensive expression profiling of the pectin methylesterase gene
RT family during silique development in Arabidopsis thaliana.";
RL Planta 224:782-791(2006).
CC -!- FUNCTION: Acts in the modification of cell walls via
CC demethylesterification of cell wall pectin. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol;
CC Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques.
CC {ECO:0000269|PubMed:16622707}.
CC -!- DEVELOPMENTAL STAGE: Expressed during late developmental phases of
CC siliques. {ECO:0000269|PubMed:16622707}.
CC -!- SIMILARITY: Belongs to the pectinesterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28786.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AP001302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE77389.1; -; Genomic_DNA.
DR EMBL; DQ653407; ABK28786.1; ALT_SEQ; mRNA.
DR RefSeq; NP_189437.1; NM_113715.1.
DR AlphaFoldDB; Q3EAY9; -.
DR SMR; Q3EAY9; -.
DR BioGRID; 7752; 1.
DR STRING; 3702.AT3G27980.1; -.
DR PaxDb; Q3EAY9; -.
DR PRIDE; Q3EAY9; -.
DR EnsemblPlants; AT3G27980.1; AT3G27980.1; AT3G27980.
DR GeneID; 822422; -.
DR Gramene; AT3G27980.1; AT3G27980.1; AT3G27980.
DR KEGG; ath:AT3G27980; -.
DR Araport; AT3G27980; -.
DR TAIR; locus:2086854; AT3G27980.
DR eggNOG; ENOG502QUQ5; Eukaryota.
DR HOGENOM; CLU_012243_9_2_1; -.
DR InParanoid; Q3EAY9; -.
DR OMA; MMESAKN; -.
DR OrthoDB; 674407at2759; -.
DR PhylomeDB; Q3EAY9; -.
DR BioCyc; ARA:AT3G27980-MON; -.
DR UniPathway; UPA00545; UER00823.
DR PRO; PR:Q3EAY9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q3EAY9; differential.
DR Genevisible; Q3EAY9; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IBA:GO_Central.
DR GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000070; Pectinesterase_cat.
DR InterPro; IPR006501; Pectinesterase_inhib_dom.
DR InterPro; IPR018040; Pectinesterase_Tyr_AS.
DR Pfam; PF01095; Pectinesterase; 1.
DR SMART; SM00856; PMEI; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS00800; PECTINESTERASE_1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl esterase; Cell wall; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..497
FT /note="Probable pectinesterase 30"
FT /id="PRO_0000370186"
FT ACT_SITE 316
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 337
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 315
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 330..350
FT /evidence="ECO:0000250"
SQ SEQUENCE 497 AA; 55459 MW; ACBB9C1E6E881284 CRC64;
MLVKVFSFFI LMIIMVIGVS KEYCDDKQSC QNLLLELKAG SSSLSEIRRR DLLIIVLKNS
VRRIDMAMIG VMDDTKQHEE MENDMLGVKE DTNLFEEMME SEENSHTWLS SVLTSYITCI
DEIGEGAYKR RVEPKLENLI SRARVVLALF ISISLRDNTE LISVIPNGPS WLFHVDKKDL
YLNAEIADVV VAKDGTGKYS TVNAAIAAAP QHSQKRFVIY IKTGIYDEIV VIENTKPNLT
LIGDGQDLTI ITGNLSASNV RRTYNTATVA SNGNGFIGVD MCFRNTAGPA KGPAVALRVS
GDMSVIYRCR VEGYQDALYP HSDRQFYREC FITGTVDFIC GNAVAVFQFC QIVARQPKMG
QSNVITAQSR ATKDVKSGFS IQNCNITTSS DLDTATVKTY LGRPWRRFST VAVLQSFIGD
LVDPAGWTPW KGETGLSTLH YREYQNRGPG AVTSRRVKWS GFKVMKDPKK ATEFTVAKLL
DGETWLKESR IPYESGL
